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1f3u

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Revision as of 07:18, 17 March 2021

CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF

Structural highlights

1f3u is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[T2FB_HUMAN] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity.^[1] [T2FA_HUMAN] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

General transcription factor IIF (TFIIF) is required for transcription by RNA polymerase II; it consists minimally of a heterodimer of RNA polymerase-associated proteins RAP30 and RAP74. According to solution and mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription initiation and elongation. The X-ray structure of the RAP30/RAP74 interaction domains at 1.7 A resolution reveals a novel "triple barrel" dimerization fold and suggests with mutant data that interactions with the transcription apparatus are mediated not only by this tripartite beta-barrel, but also via flexible loops and alpha and beta-structures extending from it.

Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.,Gaiser F, Tan S, Richmond TJ J Mol Biol. 2000 Oct 6;302(5):1119-27. PMID:11183778^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sopta M, Burton ZF, Greenblatt J. Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II. Nature. 1989 Oct 5;341(6241):410-4. PMID:2477704 doi:http://dx.doi.org/10.1038/341410a0
↑ Rossignol M, Keriel A, Staub A, Egly JM. Kinase activity and phosphorylation of the largest subunit of TFIIF transcription factor. J Biol Chem. 1999 Aug 6;274(32):22387-92. PMID:10428810
↑ Gaiser F, Tan S, Richmond TJ. Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution. J Mol Biol. 2000 Oct 6;302(5):1119-27. PMID:11183778 doi:10.1006/jmbi.2000.4110

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f3u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1f3u' size='340' side='right'caption='[[1f3u]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1f3u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F3U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1f3u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3U FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3u OCA], [http://pdbe.org/1f3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f3u RCSB], [http://www.ebi.ac.uk/pdbsum/1f3u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3u ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3u OCA], [https://pdbe.org/1f3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3u RCSB], [https://www.ebi.ac.uk/pdbsum/1f3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/T2FB_HUMAN T2FB_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity.<ref>PMID:2477704</ref>  [[http://www.uniprot.org/uniprot/T2FA_HUMAN T2FA_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.<ref>PMID:10428810</ref>
+[[https://www.uniprot.org/uniprot/T2FB_HUMAN T2FB_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity.<ref>PMID:2477704</ref>  [[https://www.uniprot.org/uniprot/T2FA_HUMAN T2FA_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.<ref>PMID:10428810</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Transcription initiation factor|Transcription initiation factor]]
+*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
 == References ==
 <references/>

1f3u

From Proteopedia

Revision as of 07:18, 17 March 2021

CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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